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P15651

- ACADS_RAT

UniProt

P15651 - ACADS_RAT

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Protein

Short-chain specific acyl-CoA dehydrogenase, mitochondrial

Gene

Acads

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

Butanoyl-CoA + electron-transfer flavoprotein = 2-butenoyl-CoA + reduced electron-transfer flavoprotein.

Cofactori

FAD.1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei161 – 1611Substrate; via carbonyl oxygen
Binding sitei297 – 2971FAD1 Publication
Binding sitei308 – 3081FADBy similarity
Active sitei392 – 3921Proton acceptor
Binding sitei393 – 3931Substrate; via amide nitrogen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi152 – 16110FAD1 Publication
Nucleotide bindingi185 – 1873FAD1 Publication
Nucleotide bindingi365 – 3695FAD1 Publication
Nucleotide bindingi394 – 3963FAD1 Publication

GO - Molecular functioni

  1. acyl-CoA dehydrogenase activity Source: RGD
  2. butyryl-CoA dehydrogenase activity Source: RGD
  3. fatty-acyl-CoA binding Source: RGD
  4. flavin adenine dinucleotide binding Source: RGD

GO - Biological processi

  1. butyrate catabolic process Source: RGD
  2. fatty acid beta-oxidation Source: RGD
  3. fatty acid beta-oxidation using acyl-CoA dehydrogenase Source: RGD
  4. protein homotetramerization Source: RGD
  5. response to glucocorticoid Source: RGD
  6. response to starvation Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

SABIO-RKP15651.
UniPathwayiUPA00660.

Names & Taxonomyi

Protein namesi
Recommended name:
Short-chain specific acyl-CoA dehydrogenase, mitochondrial (EC:1.3.8.1)
Short name:
SCAD
Alternative name(s):
Butyryl-CoA dehydrogenase
Gene namesi
Name:Acads
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620514. Acads.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: BHF-UCL
  2. mitochondrial membrane Source: BHF-UCL
  3. mitochondrion Source: RGD
  4. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2424MitochondrionAdd
BLAST
Chaini25 – 412388Short-chain specific acyl-CoA dehydrogenase, mitochondrialPRO_0000000501Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei51 – 511N6-acetyllysine; alternateBy similarity
Modified residuei51 – 511N6-succinyllysine; alternateBy similarity
Modified residuei72 – 721N6-acetyllysineBy similarity
Modified residuei129 – 1291N6-acetyllysine; alternateBy similarity
Modified residuei129 – 1291N6-succinyllysine; alternateBy similarity
Modified residuei208 – 2081N6-acetyllysineBy similarity
Modified residuei262 – 2621N6-acetyllysine; alternateBy similarity
Modified residuei262 – 2621N6-succinyllysine; alternateBy similarity
Modified residuei292 – 2921N6-acetyllysineBy similarity
Modified residuei306 – 3061N6-acetyllysine; alternateBy similarity
Modified residuei306 – 3061N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP15651.
PRIDEiP15651.

Expressioni

Gene expression databases

ExpressionAtlasiP15651. baseline.
GenevestigatoriP15651.

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

IntActiP15651. 1 interaction.
STRINGi10116.ENSRNOP00000001556.

Structurei

Secondary structure

1
412
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi36 – 5217
Turni53 – 564
Helixi57 – 637
Helixi68 – 7710
Turni78 – 803
Beta strandi81 – 844
Helixi86 – 883
Helixi95 – 10814
Helixi110 – 12112
Helixi124 – 1307
Helixi133 – 1397
Helixi141 – 1433
Beta strandi144 – 1474
Beta strandi150 – 1534
Beta strandi159 – 1624
Beta strandi169 – 1724
Beta strandi174 – 18714
Turni188 – 1914
Beta strandi193 – 2019
Helixi203 – 2086
Beta strandi209 – 21810
Beta strandi222 – 2243
Beta strandi230 – 2323
Beta strandi238 – 24912
Helixi250 – 2523
Beta strandi253 – 2564
Helixi260 – 29637
Beta strandi298 – 3036
Helixi304 – 3063
Helixi308 – 33629
Helixi342 – 36726
Helixi368 – 3714
Helixi378 – 3858
Helixi386 – 3894
Turni390 – 3923
Helixi395 – 41016

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JQIX-ray2.25A/B25-412[»]
ProteinModelPortaliP15651.
SMRiP15651. Positions 28-411.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15651.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni269 – 2724Substrate binding

Sequence similaritiesi

Belongs to the acyl-CoA dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1960.
HOVERGENiHBG000224.
InParanoidiP15651.
KOiK00248.

Family and domain databases

Gene3Di1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProiIPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view]
PfamiPF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view]
SUPFAMiSSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEiPS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15651 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAALLARAG GSLGRALRAR DWRRLHTVYQ SVELPETHQM LRQTCRDFAE
60 70 80 90 100
KELVPIAAQL DKEHLFPTSQ VKKMGELGLL AMDVPEELSG AGLDYLAYSI
110 120 130 140 150
ALEEISRGCA STGVIMSVNN SLYLGPILKF GSSQQKQQWI TPFTNGDKIG
160 170 180 190 200
CFALSEPGNG SDAGAASTTA REEGDSWVLN GTKAWITNSW EASATVVFAS
210 220 230 240 250
TDRSRQNKGI SAFLVPMPTP GLTLGKKEDK LGIRASSTAN LIFEDCRIPK
260 270 280 290 300
ENLLGEPGMG FKIAMQTLDM GRIGIASQAL GIAQASLDCA VKYAENRHAF
310 320 330 340 350
GAPLTKLQNI QFKLADMALA LESARLLTWR AAMLKDNKKP FTKESAMAKL
360 370 380 390 400
AASEAATAIS HQAIQILGGM GYVTEMPAER YYRDARITEI YEGTSEIQRL
410
VIAGHLLRSY RS
Length:412
Mass (Da):44,765
Last modified:November 1, 1995 - v2
Checksum:i3E4A052FC99B8E14
GO

Sequence cautioni

The sequence AAA40669.1 differs from that shown. Reason: Erroneous initiation.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05030 mRNA. Translation: AAA40669.1. Different initiation.
PIRiB34252.
RefSeqiNP_071957.1. NM_022512.2.
UniGeneiRn.1167.

Genome annotation databases

GeneIDi64304.
KEGGirno:64304.
UCSCiRGD:620514. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J05030 mRNA. Translation: AAA40669.1 . Different initiation.
PIRi B34252.
RefSeqi NP_071957.1. NM_022512.2.
UniGenei Rn.1167.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JQI X-ray 2.25 A/B 25-412 [» ]
ProteinModelPortali P15651.
SMRi P15651. Positions 28-411.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P15651. 1 interaction.
STRINGi 10116.ENSRNOP00000001556.

Chemistry

ChEMBLi CHEMBL2176825.

Proteomic databases

PaxDbi P15651.
PRIDEi P15651.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 64304.
KEGGi rno:64304.
UCSCi RGD:620514. rat.

Organism-specific databases

CTDi 35.
RGDi 620514. Acads.

Phylogenomic databases

eggNOGi COG1960.
HOVERGENi HBG000224.
InParanoidi P15651.
KOi K00248.

Enzyme and pathway databases

UniPathwayi UPA00660 .
SABIO-RK P15651.

Miscellaneous databases

EvolutionaryTracei P15651.
NextBioi 612942.
PROi P15651.

Gene expression databases

ExpressionAtlasi P15651. baseline.
Genevestigatori P15651.

Family and domain databases

Gene3Di 1.10.540.10. 1 hit.
2.40.110.10. 1 hit.
InterProi IPR006089. Acyl-CoA_DH_CS.
IPR006091. Acyl-CoA_Oxase/DH_cen-dom.
IPR009075. AcylCo_DH/oxidase_C.
IPR013786. AcylCoA_DH/ox_N.
IPR009100. AcylCoA_DH/oxidase_NM_dom.
[Graphical view ]
Pfami PF00441. Acyl-CoA_dh_1. 1 hit.
PF02770. Acyl-CoA_dh_M. 1 hit.
PF02771. Acyl-CoA_dh_N. 1 hit.
[Graphical view ]
SUPFAMi SSF47203. SSF47203. 1 hit.
SSF56645. SSF56645. 1 hit.
PROSITEi PS00072. ACYL_COA_DH_1. 1 hit.
PS00073. ACYL_COA_DH_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Molecular cloning and nucleotide sequence of cDNAs encoding the precursors of rat long chain acyl-coenzyme A, short chain acyl-coenzyme A, and isovaleryl-coenzyme A dehydrogenases. Sequence homology of four enzymes of the acyl-CoA dehydrogenase family."
    Matsubara Y., Indo Y., Naito E., Ozasa H., Glassberg R., Vockley J., Ikeda Y., Kraus J., Tanaka K.
    J. Biol. Chem. 264:16321-16331(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. "Crystal structure of rat short chain acyl-CoA dehydrogenase complexed with acetoacetyl-CoA: comparison with other acyl-CoA dehydrogenases."
    Battaile K.P., Molin-Case J., Paschke R., Wang M., Bennett D., Vockley J., Kim J.-J.P.
    J. Biol. Chem. 277:12200-12207(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 25-412 IN COMPLEX WITH THE SUBSTRATE ANALOG ACETOACETYL-COA AND FAD, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiACADS_RAT
AccessioniPrimary (citable) accession number: P15651
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1995
Last modified: October 29, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

A number of straight-chain acyl-CoA dehydrogenases of different substrate specificities are present in mammalian tissues.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3